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Purification and characterization of histone H1 variants from human placenta

Pyo, Sang-Hyun LU orcid ; Lee, Jae-Heung ; Lee, Yeune Hee ; Yoon, Jong-Won and Kim, Jin-Hyun (2008) In Biotechnology and Bioprocess Engineering 13. p.772-777
Abstract
Three histone H1 variants were extracted from human placental tissue in a single process using a high-salt buffer solution, and purified by ion exchange, hydroxyapatite, and reversed-phase chromatography. In the first chromatographic step, a cation exchanger resin, SP-Sepharose FF, was used to remove impurities having molecular weights higher than those of histones. In the second chromatographic step, hydroxyapatite resin was used to remove impurities with relatively low molecular weights. A second round of cation exchange chromatography using high-grade HS POROS resin resulted in two main fractions, each of which appeared as a single band following SDS-PAGE. The first fraction showed a single peak in RP-HPLC, while the second fraction... (More)
Three histone H1 variants were extracted from human placental tissue in a single process using a high-salt buffer solution, and purified by ion exchange, hydroxyapatite, and reversed-phase chromatography. In the first chromatographic step, a cation exchanger resin, SP-Sepharose FF, was used to remove impurities having molecular weights higher than those of histones. In the second chromatographic step, hydroxyapatite resin was used to remove impurities with relatively low molecular weights. A second round of cation exchange chromatography using high-grade HS POROS resin resulted in two main fractions, each of which appeared as a single band following SDS-PAGE. The first fraction showed a single peak in RP-HPLC, while the second fraction showed two main peaks. These three peaks were further separated and polished by semi-preparative RP-HPLC, and their molecular masses and sequences were determined using MALDI-TOF-MS and N-terminal amino acid sequencing, respectively. The sequences and masses of these three variants corresponded with those of histones H1.2, H1.4, and H1.5. Moreover, all three purified histone subtypes demonstrated cytotoxicity in an MTT assay. (Less)
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author
; ; ; and
publishing date
type
Contribution to journal
publication status
published
subject
in
Biotechnology and Bioprocess Engineering
volume
13
pages
772 - 777
publisher
Korean Society for Biotechnology and Bioengineering
external identifiers
  • scopus:59849096865
ISSN
1226-8372
DOI
10.1007/s12257-008-0186-1
language
English
LU publication?
no
id
83449036-979b-40a4-8bc6-a992ac1cc656
date added to LUP
2025-09-19 11:26:10
date last changed
2025-10-14 09:43:39
@article{83449036-979b-40a4-8bc6-a992ac1cc656,
  abstract     = {{Three histone H1 variants were extracted from human placental tissue in a single process using a high-salt buffer solution, and purified by ion exchange, hydroxyapatite, and reversed-phase chromatography. In the first chromatographic step, a cation exchanger resin, SP-Sepharose FF, was used to remove impurities having molecular weights higher than those of histones. In the second chromatographic step, hydroxyapatite resin was used to remove impurities with relatively low molecular weights. A second round of cation exchange chromatography using high-grade HS POROS resin resulted in two main fractions, each of which appeared as a single band following SDS-PAGE. The first fraction showed a single peak in RP-HPLC, while the second fraction showed two main peaks. These three peaks were further separated and polished by semi-preparative RP-HPLC, and their molecular masses and sequences were determined using MALDI-TOF-MS and N-terminal amino acid sequencing, respectively. The sequences and masses of these three variants corresponded with those of histones H1.2, H1.4, and H1.5. Moreover, all three purified histone subtypes demonstrated cytotoxicity in an MTT assay.}},
  author       = {{Pyo, Sang-Hyun and Lee, Jae-Heung and Lee, Yeune Hee and Yoon, Jong-Won and Kim, Jin-Hyun}},
  issn         = {{1226-8372}},
  language     = {{eng}},
  pages        = {{772--777}},
  publisher    = {{Korean Society for Biotechnology and Bioengineering}},
  series       = {{Biotechnology and Bioprocess Engineering}},
  title        = {{Purification and characterization of histone H1 variants from human placenta}},
  url          = {{http://dx.doi.org/10.1007/s12257-008-0186-1}},
  doi          = {{10.1007/s12257-008-0186-1}},
  volume       = {{13}},
  year         = {{2008}},
}